Protein structure evolution in liquid DESI as revealed by selective noncovalent adduct protein probing.

ABSTRACT: Previous experiments based on charge state distributions have suggested that liquid desorption electrospray ionization (DESI) is capable of preserving solution phase protein structure during transfer to the gas phase (Journal of the American Society for Mass Spectrometry 21 (2010) 1730-1736). In order to examine this possibility more carefully, we have utilized selective non-covalent adduct protein probing (SNAPP) to evaluate protein structural evolution in both liquid DESI and standard ESI under a variety of conditions. Experiments with cytochrome c (Cytc) demonstrated that methanol induced conformational shifts previously observed with ESI are also easily observed with liquid DESI. However, undesirable acid-induced unfolding becomes apparent at very high concentrations of methanol in liq

SUBMITTER: Moore BN 

PROVIDER: S-EPMC3601934 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature